HEADER METAL TRANSPORT 17-FEB-17 5X5P
TITLE HUMAN SERUM TRANSFERRIN BOUND TO RUTHENIUM NTA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEROTRANSFERRIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSFERRIN,BETA-1 METAL-BINDING GLOBULIN,SIDEROPHILIN;
COMPND 5 OTHER_DETAILS: HUMAN SERUM TRANSFERRIN FROM SIGMA. (CAT.NO. T2036)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TRANSFERRIN, RUTHENIUM, NTA, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SUN,M.WANG
REVDAT 4 22-NOV-23 5X5P 1 REMARK
REVDAT 3 15-NOV-23 5X5P 1 LINK ATOM
REVDAT 2 22-JUN-22 5X5P 1 JRNL REMARK LINK
REVDAT 1 21-FEB-18 5X5P 0
JRNL AUTH M.WANG,H.WANG,X.XU,T.P.LAI,Y.ZHOU,Q.HAO,H.LI,H.SUN
JRNL TITL BINDING OF RUTHENIUM AND OSMIUM AT NON‐IRON SITES OF
JRNL TITL 2 TRANSFERRIN ACCOUNTS FOR THEIR IRON-INDEPENDENT CELLULAR
JRNL TITL 3 UPTAKE.
JRNL REF J.INORG.BIOCHEM. V. 234 11885 2022
JRNL REFN ISSN 0162-0134
JRNL PMID 35690040
JRNL DOI 10.1016/J.JINORGBIO.2022.111885
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 32206
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1628
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2158
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4969
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 9
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.06000
REMARK 3 B22 (A**2) : -2.69000
REMARK 3 B33 (A**2) : 3.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.244
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.783
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5125 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4595 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6939 ; 1.209 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10702 ; 0.933 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 645 ; 5.419 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 223 ;37.307 ;24.529
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 842 ;16.980 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;15.564 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 744 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5753 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1022 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5087 ; 6.245 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4961 ;44.879 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 92
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5854 10.3086 -13.1904
REMARK 3 T TENSOR
REMARK 3 T11: 0.1191 T22: 0.1217
REMARK 3 T33: 0.0155 T12: -0.0066
REMARK 3 T13: 0.0090 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.7645 L22: 0.0202
REMARK 3 L33: 0.0360 L12: 0.0313
REMARK 3 L13: 0.1613 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0425 S12: -0.0040 S13: 0.0107
REMARK 3 S21: -0.0150 S22: 0.0319 S23: -0.0127
REMARK 3 S31: -0.0053 S32: -0.0048 S33: 0.0106
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 93 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9122 18.9303 18.4814
REMARK 3 T TENSOR
REMARK 3 T11: 0.0981 T22: 0.1124
REMARK 3 T33: 0.0025 T12: -0.0018
REMARK 3 T13: 0.0064 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.3044 L22: 1.1666
REMARK 3 L33: 0.1037 L12: -0.1580
REMARK 3 L13: 0.1737 L23: -0.1546
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: -0.0090 S13: 0.0068
REMARK 3 S21: 0.0011 S22: -0.0022 S23: 0.0418
REMARK 3 S31: 0.0111 S32: -0.0047 S33: -0.0006
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 247 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6562 16.6504 -8.6703
REMARK 3 T TENSOR
REMARK 3 T11: 0.0981 T22: 0.1362
REMARK 3 T33: 0.0140 T12: -0.0102
REMARK 3 T13: -0.0056 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.3210 L22: 0.1221
REMARK 3 L33: 0.0437 L12: -0.1965
REMARK 3 L13: 0.1176 L23: -0.0714
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: 0.0329 S13: 0.0026
REMARK 3 S21: 0.0006 S22: -0.0019 S23: -0.0031
REMARK 3 S31: -0.0033 S32: 0.0184 S33: 0.0058
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 339 A 425
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5646 35.2185 0.7668
REMARK 3 T TENSOR
REMARK 3 T11: 0.1230 T22: 0.1268
REMARK 3 T33: 0.0803 T12: -0.0650
REMARK 3 T13: -0.0254 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 0.7092 L22: 1.6735
REMARK 3 L33: 1.7460 L12: -0.5368
REMARK 3 L13: 0.0410 L23: -0.4516
REMARK 3 S TENSOR
REMARK 3 S11: 0.1285 S12: -0.0630 S13: -0.1381
REMARK 3 S21: 0.0316 S22: -0.0940 S23: -0.1257
REMARK 3 S31: -0.0700 S32: 0.1392 S33: -0.0344
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 426 A 577
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0101 56.2105 -15.2237
REMARK 3 T TENSOR
REMARK 3 T11: 0.1040 T22: 0.1215
REMARK 3 T33: 0.0102 T12: -0.0135
REMARK 3 T13: -0.0021 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.3221 L22: 0.8925
REMARK 3 L33: 0.0242 L12: 0.4156
REMARK 3 L13: -0.1565 L23: -0.1071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0741 S12: 0.0084 S13: 0.0529
REMARK 3 S21: 0.0859 S22: -0.0608 S23: 0.0855
REMARK 3 S31: -0.0039 S32: -0.0025 S33: -0.0133
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 581 A 679
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8835 41.6879 2.7915
REMARK 3 T TENSOR
REMARK 3 T11: 0.1131 T22: 0.1391
REMARK 3 T33: 0.0141 T12: -0.0423
REMARK 3 T13: 0.0271 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.0361 L22: 1.2078
REMARK 3 L33: 1.3139 L12: 0.0640
REMARK 3 L13: -0.0000 L23: -0.5213
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: -0.0631 S13: 0.0144
REMARK 3 S21: 0.1925 S22: -0.0555 S23: 0.0012
REMARK 3 S31: -0.2215 S32: 0.0946 S33: 0.0222
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5X5P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300002445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.14026
REMARK 200 MONOCHROMATOR : GRAPHITE FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32206
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.63600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3QYT
REMARK 200
REMARK 200 REMARK: HALF-MOON LIKE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PIPES-NA 100MM PH 6.6, DISODIUM
REMARK 280 MALONATE 8MM, PEG 3350 18%, GLYCEROL 17%, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.30500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.30500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 68.37400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 79.19750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 68.37400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 79.19750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.30500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 68.37400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 79.19750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.30500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 68.37400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 79.19750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 333
REMARK 465 ALA A 334
REMARK 465 PRO A 335
REMARK 465 THR A 336
REMARK 465 ASP A 337
REMARK 465 GLU A 338
REMARK 465 LYS A 414
REMARK 465 SER A 415
REMARK 465 ASP A 416
REMARK 465 ASN A 417
REMARK 465 CYS A 418
REMARK 465 GLU A 419
REMARK 465 ASP A 420
REMARK 465 THR A 421
REMARK 465 PRO A 422
REMARK 465 GLU A 423
REMARK 465 VAL A 612
REMARK 465 THR A 613
REMARK 465 ASP A 614
REMARK 465 CYS A 615
REMARK 465 SER A 616
REMARK 465 GLY A 617
REMARK 465 ASN A 618
REMARK 465 PHE A 619
REMARK 465 CYS A 620
REMARK 465 LEU A 621
REMARK 465 PHE A 622
REMARK 465 ARG A 623
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 89 CG CD OE1 OE2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 HIS A 350 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 363 CG1 CG2
REMARK 470 LYS A 365 CG CD CE NZ
REMARK 470 LYS A 470 CG CD CE NZ
REMARK 470 LYS A 599 CG CD CE NZ
REMARK 470 ARG A 602 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 606 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 611 CG OD1 ND2
REMARK 470 GLU A 625 CG CD OE1 OE2
REMARK 470 ARG A 632 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 640 CG CD CE NZ
REMARK 470 HIS A 642 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 653 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR A 188 O HOH A 801 2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 201 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 522 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 29 -37.28 -130.00
REMARK 500 PRO A 31 -172.80 -69.96
REMARK 500 SER A 125 -70.87 -72.78
REMARK 500 TRP A 128 -65.65 -148.23
REMARK 500 CYS A 179 35.45 -91.53
REMARK 500 CYS A 241 82.58 -160.32
REMARK 500 ALA A 244 149.53 -173.71
REMARK 500 LYS A 259 71.06 -107.86
REMARK 500 LEU A 294 -42.99 72.48
REMARK 500 LYS A 340 157.35 69.06
REMARK 500 ALA A 436 84.82 -69.82
REMARK 500 ALA A 453 159.43 178.33
REMARK 500 TRP A 460 -62.17 -149.15
REMARK 500 LYS A 527 -40.30 -134.05
REMARK 500 GLU A 573 43.75 -102.46
REMARK 500 THR A 626 -97.20 -83.43
REMARK 500 LEU A 630 -60.17 68.53
REMARK 500 HIS A 642 -99.60 58.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 RU A 703 RU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 14 NE2
REMARK 620 2 NTA A 707 O8 105.4
REMARK 620 3 NTA A 707 N 86.7 96.3
REMARK 620 4 NTA A 707 OXT 84.1 168.1 91.3
REMARK 620 5 HOH A 803 O 132.2 82.5 140.2 85.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 709 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 125 OG
REMARK 620 2 TYR A 319 OH 116.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 RU A 705 RU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 273 NE2
REMARK 620 2 HOH A 804 O 70.5
REMARK 620 3 HOH A 808 O 100.2 162.3
REMARK 620 4 HOH A 809 O 86.5 78.5 86.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 702 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 392 OD2
REMARK 620 2 TYR A 426 OH 97.0
REMARK 620 3 TYR A 517 OH 172.0 84.5
REMARK 620 4 HIS A 585 NE2 105.1 93.4 82.6
REMARK 620 5 MLI A 701 O7 84.5 95.4 87.5 166.1
REMARK 620 6 MLI A 701 O9 93.3 169.4 84.9 86.2 83.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 RU A 704 RU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 578 NE2
REMARK 620 2 NTA A 708 O 100.1
REMARK 620 3 NTA A 708 N 173.7 79.8
REMARK 620 4 NTA A 708 O13 112.5 77.2 73.6
REMARK 620 5 NTA A 708 O9 86.7 157.0 95.9 79.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RU A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RU A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RU A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RU A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NTA A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NTA A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 709
DBREF 5X5P A 1 679 UNP P02787 TRFE_HUMAN 20 698
SEQRES 1 A 679 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 A 679 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 A 679 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 A 679 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 A 679 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 A 679 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 A 679 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 A 679 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 A 679 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 A 679 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 A 679 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 A 679 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 A 679 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 A 679 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 A 679 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 A 679 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL LYS HIS SER
SEQRES 17 A 679 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 A 679 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 A 679 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 A 679 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 A 679 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 A 679 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 A 679 SER PRO HIS GLY LYS ASP LEU LEU PHE LYS ASP SER ALA
SEQRES 24 A 679 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 A 679 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 A 679 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP GLU
SEQRES 27 A 679 CYS LYS PRO VAL LYS TRP CYS ALA LEU SER HIS HIS GLU
SEQRES 28 A 679 ARG LEU LYS CYS ASP GLU TRP SER VAL ASN SER VAL GLY
SEQRES 29 A 679 LYS ILE GLU CYS VAL SER ALA GLU THR THR GLU ASP CYS
SEQRES 30 A 679 ILE ALA LYS ILE MET ASN GLY GLU ALA ASP ALA MET SER
SEQRES 31 A 679 LEU ASP GLY GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY
SEQRES 32 A 679 LEU VAL PRO VAL LEU ALA GLU ASN TYR ASN LYS SER ASP
SEQRES 33 A 679 ASN CYS GLU ASP THR PRO GLU ALA GLY TYR PHE ALA ILE
SEQRES 34 A 679 ALA VAL VAL LYS LYS SER ALA SER ASP LEU THR TRP ASP
SEQRES 35 A 679 ASN LEU LYS GLY LYS LYS SER CYS HIS THR ALA VAL GLY
SEQRES 36 A 679 ARG THR ALA GLY TRP ASN ILE PRO MET GLY LEU LEU TYR
SEQRES 37 A 679 ASN LYS ILE ASN HIS CYS ARG PHE ASP GLU PHE PHE SER
SEQRES 38 A 679 GLU GLY CYS ALA PRO GLY SER LYS LYS ASP SER SER LEU
SEQRES 39 A 679 CYS LYS LEU CYS MET GLY SER GLY LEU ASN LEU CYS GLU
SEQRES 40 A 679 PRO ASN ASN LYS GLU GLY TYR TYR GLY TYR THR GLY ALA
SEQRES 41 A 679 PHE ARG CYS LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL
SEQRES 42 A 679 LYS HIS GLN THR VAL PRO GLN ASN THR GLY GLY LYS ASN
SEQRES 43 A 679 PRO ASP PRO TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR
SEQRES 44 A 679 GLU LEU LEU CYS LEU ASP GLY THR ARG LYS PRO VAL GLU
SEQRES 45 A 679 GLU TYR ALA ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS
SEQRES 46 A 679 ALA VAL VAL THR ARG LYS ASP LYS GLU ALA CYS VAL HIS
SEQRES 47 A 679 LYS ILE LEU ARG GLN GLN GLN HIS LEU PHE GLY SER ASN
SEQRES 48 A 679 VAL THR ASP CYS SER GLY ASN PHE CYS LEU PHE ARG SER
SEQRES 49 A 679 GLU THR LYS ASP LEU LEU PHE ARG ASP ASP THR VAL CYS
SEQRES 50 A 679 LEU ALA LYS LEU HIS ASP ARG ASN THR TYR GLU LYS TYR
SEQRES 51 A 679 LEU GLY GLU GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG
SEQRES 52 A 679 LYS CYS SER THR SER SER LEU LEU GLU ALA CYS THR PHE
SEQRES 53 A 679 ARG ARG PRO
HET MLI A 701 7
HET FE A 702 1
HET RU A 703 1
HET RU A 704 1
HET RU A 705 1
HET RU A 706 1
HET NTA A 707 13
HET NTA A 708 13
HET NA A 709 1
HETNAM MLI MALONATE ION
HETNAM FE FE (III) ION
HETNAM RU RUTHENIUM ION
HETNAM NTA NITRILOTRIACETIC ACID
HETNAM NA SODIUM ION
FORMUL 2 MLI C3 H2 O4 2-
FORMUL 3 FE FE 3+
FORMUL 4 RU 4(RU 3+)
FORMUL 8 NTA 2(C6 H9 N O6)
FORMUL 10 NA NA 1+
FORMUL 11 HOH *9(H2 O)
HELIX 1 AA1 SER A 12 LYS A 27 1 16
HELIX 2 AA2 SER A 44 ALA A 54 1 11
HELIX 3 AA3 ASP A 63 LEU A 72 1 10
HELIX 4 AA4 GLN A 108 LEU A 112 5 5
HELIX 5 AA5 TRP A 128 TYR A 136 1 9
HELIX 6 AA6 CYS A 137 LEU A 139 5 3
HELIX 7 AA7 PRO A 145 ASN A 152 1 8
HELIX 8 AA8 PHE A 167 GLN A 172 5 6
HELIX 9 AA9 PHE A 186 ASP A 197 1 12
HELIX 10 AB1 SER A 208 LEU A 214 1 7
HELIX 11 AB2 ASN A 216 ASP A 221 1 6
HELIX 12 AB3 PRO A 234 CYS A 241 5 8
HELIX 13 AB4 LYS A 259 GLY A 275 1 17
HELIX 14 AB5 ASP A 310 GLY A 316 1 7
HELIX 15 AB6 GLY A 316 GLY A 329 1 14
HELIX 16 AB7 SER A 348 ASN A 361 1 14
HELIX 17 AB8 THR A 373 GLY A 384 1 12
HELIX 18 AB9 ASP A 392 CYS A 402 1 11
HELIX 19 AC1 TRP A 460 ASN A 472 1 13
HELIX 20 AC2 ARG A 475 PHE A 479 5 5
HELIX 21 AC3 SER A 492 LYS A 496 5 5
HELIX 22 AC4 SER A 501 LEU A 505 5 5
HELIX 23 AC5 TYR A 515 LYS A 527 1 13
HELIX 24 AC6 GLN A 536 ASN A 541 1 6
HELIX 25 AC7 ASP A 548 ASN A 553 1 6
HELIX 26 AC8 ASN A 555 LYS A 557 5 3
HELIX 27 AC9 GLU A 573 CYS A 577 5 5
HELIX 28 AD1 ARG A 590 ASP A 592 5 3
HELIX 29 AD2 LYS A 593 GLY A 609 1 17
HELIX 30 AD3 THR A 646 GLY A 652 1 7
HELIX 31 AD4 GLY A 652 ARG A 663 1 12
HELIX 32 AD5 SER A 668 ARG A 678 1 11
SHEET 1 AA1 2 THR A 5 ALA A 10 0
SHEET 2 AA1 2 SER A 36 LYS A 41 1 O ALA A 38 N TRP A 8
SHEET 1 AA2 4 VAL A 60 LEU A 62 0
SHEET 2 AA2 4 THR A 250 ARG A 254 -1 O THR A 250 N LEU A 62
SHEET 3 AA2 4 LEU A 77 PHE A 84 -1 N LYS A 78 O ALA A 253
SHEET 4 AA2 4 GLY A 301 LYS A 304 -1 O LEU A 303 N ALA A 82
SHEET 1 AA3 6 GLY A 156 CYS A 158 0
SHEET 2 AA3 6 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 AA3 6 VAL A 202 LYS A 206 1 O VAL A 202 N CYS A 118
SHEET 4 AA3 6 PHE A 94 LYS A 102 -1 N VAL A 98 O VAL A 205
SHEET 5 AA3 6 TYR A 223 LEU A 226 -1 O GLU A 224 N VAL A 101
SHEET 6 AA3 6 ARG A 232 LYS A 233 -1 O LYS A 233 N LEU A 225
SHEET 1 AA4 5 GLY A 156 CYS A 158 0
SHEET 2 AA4 5 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 AA4 5 VAL A 202 LYS A 206 1 O VAL A 202 N CYS A 118
SHEET 4 AA4 5 PHE A 94 LYS A 102 -1 N VAL A 98 O VAL A 205
SHEET 5 AA4 5 ALA A 244 PRO A 247 -1 O VAL A 246 N TYR A 95
SHEET 1 AA5 2 VAL A 342 ALA A 346 0
SHEET 2 AA5 2 ILE A 366 SER A 370 1 O VAL A 369 N TRP A 344
SHEET 1 AA6 4 MET A 389 LEU A 391 0
SHEET 2 AA6 4 ALA A 586 THR A 589 -1 O ALA A 586 N LEU A 391
SHEET 3 AA6 4 VAL A 405 ASN A 411 -1 N LEU A 408 O VAL A 587
SHEET 4 AA6 4 CYS A 637 ALA A 639 -1 O ALA A 639 N ALA A 409
SHEET 1 AA7 6 GLU A 482 CYS A 484 0
SHEET 2 AA7 6 LYS A 448 HIS A 451 1 N HIS A 451 O CYS A 484
SHEET 3 AA7 6 VAL A 530 LYS A 534 1 O PHE A 532 N CYS A 450
SHEET 4 AA7 6 TYR A 426 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 AA7 6 TYR A 559 LEU A 562 -1 O GLU A 560 N VAL A 432
SHEET 6 AA7 6 ARG A 568 PRO A 570 -1 O LYS A 569 N LEU A 561
SHEET 1 AA8 5 GLU A 482 CYS A 484 0
SHEET 2 AA8 5 LYS A 448 HIS A 451 1 N HIS A 451 O CYS A 484
SHEET 3 AA8 5 VAL A 530 LYS A 534 1 O PHE A 532 N CYS A 450
SHEET 4 AA8 5 TYR A 426 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 AA8 5 ALA A 580 ALA A 582 -1 O ALA A 582 N TYR A 426
SSBOND 1 CYS A 9 CYS A 48 1555 1555 2.18
SSBOND 2 CYS A 19 CYS A 39 1555 1555 2.17
SSBOND 3 CYS A 118 CYS A 194 1555 1555 2.06
SSBOND 4 CYS A 137 CYS A 331 1555 1555 2.10
SSBOND 5 CYS A 158 CYS A 174 1555 1555 2.01
SSBOND 6 CYS A 161 CYS A 179 1555 1555 2.04
SSBOND 7 CYS A 171 CYS A 177 1555 1555 1.97
SSBOND 8 CYS A 227 CYS A 241 1555 1555 2.06
SSBOND 9 CYS A 339 CYS A 596 1555 1555 2.06
SSBOND 10 CYS A 345 CYS A 377 1555 1555 2.05
SSBOND 11 CYS A 355 CYS A 368 1555 1555 2.06
SSBOND 12 CYS A 402 CYS A 674 1555 1555 1.96
SSBOND 13 CYS A 450 CYS A 523 1555 1555 2.05
SSBOND 14 CYS A 474 CYS A 665 1555 1555 2.08
SSBOND 15 CYS A 484 CYS A 498 1555 1555 2.07
SSBOND 16 CYS A 495 CYS A 506 1555 1555 2.06
SSBOND 17 CYS A 563 CYS A 577 1555 1555 2.04
LINK NE2 HIS A 14 RU RU A 703 1555 1555 2.13
LINK OG SER A 125 NA NA A 709 1555 1555 2.90
LINK NE2 HIS A 273 RU RU A 705 1555 1555 2.32
LINK NE2 HIS A 289 RU RU A 706 1555 1555 2.40
LINK OH TYR A 319 NA NA A 709 1555 1555 3.06
LINK OD2 ASP A 392 FE FE A 702 1555 1555 2.17
LINK OH TYR A 426 FE FE A 702 1555 1555 2.25
LINK OH TYR A 517 FE FE A 702 1555 1555 2.02
LINK NE2 HIS A 578 RU RU A 704 1555 1555 1.83
LINK NE2 HIS A 585 FE FE A 702 1555 1555 2.40
LINK O7 MLI A 701 FE FE A 702 1555 1555 1.97
LINK O9 MLI A 701 FE FE A 702 1555 1555 1.95
LINK RU RU A 703 O8 NTA A 707 1555 1555 1.81
LINK RU RU A 703 N NTA A 707 1555 1555 2.18
LINK RU RU A 703 OXT NTA A 707 1555 1555 2.41
LINK RU RU A 703 O HOH A 803 1555 1555 2.19
LINK RU RU A 704 O NTA A 708 1555 1555 2.24
LINK RU RU A 704 N NTA A 708 1555 1555 1.79
LINK RU RU A 704 O13 NTA A 708 1555 1555 2.46
LINK RU RU A 704 O9 NTA A 708 1555 1555 1.78
LINK RU RU A 705 O HOH A 804 1555 1555 2.36
LINK RU RU A 705 O HOH A 808 1555 3554 2.71
LINK RU RU A 705 O HOH A 809 1555 1555 2.27
CISPEP 1 ALA A 73 PRO A 74 0 1.26
CISPEP 2 GLU A 141 PRO A 142 0 -1.60
CISPEP 3 LYS A 144 PRO A 145 0 -4.26
CISPEP 4 GLY A 258 LYS A 259 0 4.80
SITE 1 AC1 10 ASP A 392 TYR A 426 THR A 452 ARG A 456
SITE 2 AC1 10 THR A 457 ALA A 458 GLY A 459 TYR A 517
SITE 3 AC1 10 HIS A 585 FE A 702
SITE 1 AC2 5 ASP A 392 TYR A 426 TYR A 517 HIS A 585
SITE 2 AC2 5 MLI A 701
SITE 1 AC3 3 HIS A 14 NTA A 707 HOH A 803
SITE 1 AC4 2 HIS A 578 NTA A 708
SITE 1 AC5 4 HIS A 273 HOH A 804 HOH A 808 HOH A 809
SITE 1 AC6 1 HIS A 289
SITE 1 AC7 4 HIS A 14 HIS A 289 RU A 703 HOH A 803
SITE 1 AC8 3 HIS A 578 ARG A 581 RU A 704
SITE 1 AC9 3 SER A 125 ASN A 129 TYR A 319
CRYST1 136.748 158.395 106.610 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007313 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009380 0.00000
(ATOM LINES ARE NOT SHOWN.)
END